Nanopore sensing of single-biomolecules: a new procedure to identify protein sequence motifs from molecular dynamics

Nanoscale ◽  
2020 ◽  
Vol 12 (44) ◽  
pp. 22743-22753
Author(s):  
Adrien Nicolaï ◽  
Aniket Rath ◽  
Patrice Delarue ◽  
Patrick Senet
Keyword(s):  
Molecular Dynamics ◽  
Solid State ◽  
Protein Sequence ◽  
Sequence Motifs ◽  
Protein Sequence Motifs

MoS2 nanopores have emerged as one of the most promising solid-state nanopores for protein sequence motifs detection.

Early Molecular Evolution

2006 ◽  
Vol 52 (3-4) ◽  
pp. 375-387 ◽  
Author(s):  
Edward N. Trifonov
Keyword(s):  
Molecular Evolution ◽  
Protein Sequence ◽  
Last Common Ancestor ◽  
Sequence Motifs ◽  
Molecular Events ◽  
Function Modules ◽  
Recent Developments ◽  
Module Size ◽  
Protein Sequence Motifs ◽  
Polypeptide Chains

Four fundamentally novel, recent developments make a basis for the Theory of Early Molecular Evolution. The theory outlines the molecular events from the onset of the triplet code to the formation of the earliest sequence/structure/function modules of proteins. These developments are: (1) Reconstruction of the evolutionary chart of codons; (2) Discovery of omnipresent protein sequence motifs, apparently conserved since the last common ancestor; (3) Discovery of closed loops—standard structural modules of modern proteins; (4) Construction of protein sequence space of module size fragments, with far-reaching evolutionary implications. The theory generates numerous predictions, confirmed by massive nucleotide and protein sequence analyses, such as existence of two distinct classes of amino acids, and their periodical distribution along the sequences. The emerging picture of the earliest molecular evolutionary events is outlined: consecutive engagement of codons, formation of the earliest short peptides, and growth of the polypeptide chains to the size of loop closure, 25-30 residues.

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